Characterization of a Highly Purified, Fully Active, Crystallizable RC–LH1–PufX Core Complex from Rhodobacter sphaeroides-Reference-Cited by-同舟云学术

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Characterization of a Highly Purified, Fully Active, Crystallizable RC–LH1–PufX Core Complex from Rhodobacter sphaeroides

Published:2005-11 Issue:1-2 Volume:86 Page:61-70
ISSN:0166-8595
Container-title:Photosynthesis Research
language:en
Short-container-title:Photosynth Res

Author:

Abresch E.C.,Axelrod H.L.A.,Beatty J.T.,Johnson J.A.,Nechushtai R.,Paddock M.L.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Plant Science,Biochemistry,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s11120-005-5106-z.pdf

Reference42 articles.

1. The native architecture of a photosynthetic membrane

2. Flexibility and Size Heterogeneity of the LH1 Light Harvesting Complex Revealed by Atomic Force Microscopy

3. Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex.

4. Anoxygenic Photosynthetic Bacteria

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2. An LH1–RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins;Communications Biology;2022-11-07

3. Bio-Phototransistors with Immobilized Photosynthetic Proteins;Electronics;2020-10-18

4. New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins;eLife;2020-03-03

5. Large Photocurrent Response and External Quantum Efficiency in Biophotoelectrochemical Cells Incorporating Reaction Center Plus Light Harvesting Complexes;Biomacromolecules;2015-03-30

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